4 results match your criteria: "Centre of Marine Biotechnology[Affiliation]"
Mar Pollut Bull
April 2020
Inter-University Centre of Marine Biotechnology, School of Marine Sciences, CUSAT, Kochi, PIN-682016, Kerala, India.
Core sediment samples were collected from five mangrove ecosystems along northern Kerala coast (Kunjimangalam: S1, Pazhayangadi: S2, Pappinissery: S3, Thalassery: S4, and Kadalundi: S5) to assess the status of heavy metal pollution. S1 recorded comparatively lower metal concentration at surface (except Pb) due to low organic content and sandy texture, while the reverse was true for S3. Higher metal contents were recorded at S5 (0-5 cm), which was attributed to its unique biogeochemical behavior.
View Article and Find Full Text PDFAntonie Van Leeuwenhoek
April 2013
UNESCO Chinese Centre of Marine Biotechnology, Ocean University of China, Yushan Road, No. 5, Qingdao, China.
In our previous study, it was found that the killer toxin produced by the marine-derived yeast Wickerhamomyces anomalus YF07b has both killing activity and β-1,3-glucanase activity and the molecular mass of it is 47.0 kDa. In this study, the same yeast strain was found to produce another killer toxin which only had killing activity against some yeast strains, but had no β-1,3-glucanase activity and the molecular mass of the purified killer toxin was 67.
View Article and Find Full Text PDFAppl Microbiol Biotechnol
September 2011
UNESCO Chinese Centre of Marine Biotechnology, Ocean University of China, Yushan Road, No. 5, Qingdao, China.
The yeast Kluyveromyces siamensis HN12-1 isolated from mangrove ecosystem was found to be able to produce killer toxin against the pathogenic yeast (Metschnikowia bicuspidata WCY) in crab. When the killer yeast was grown in the medium with pH 4.0 and 0.
View Article and Find Full Text PDFPrep Biochem
February 1994
Norwegian Institute of Fisheries and Aquaculture, Centre of Marine Biotechnology, Tromsø.
A crude lysozyme preparation was recovered in waste from the scallop processing industry. Lysozyme was then purified 229-fold in preparative scale by chromatography on S Sepharose and Blue Sepharose. Further purification on Sephacryl S-200 resulted in a lysozyme preparation with a specific activity of 64,000 units/mg protein.
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